Tropomyosin-troponin complex stabilizes the pointed ends of actin filaments against polymerization and depolymerization.
In striated muscle the pointed ends of polar actin filaments are directed toward the center of the sarcomere. Formed filaments keep a constant length of about 1 micron. As polymerization and depolymerization at free pointed ends are not sufficiently slow to account for the constant length of the filaments, we searched for proteins which occur in sarcomeres and can stabilize the pointed ends of actin filaments. We observed that tropomyosin-troponin complex reduces the rate of association and dissociation of actin molecules at the pointed ends more than 30-fold. On the average, every 600 s one association or dissociation reaction has been found to occur at the pointed ends near the critical actin monomer concentration.
Weigt
C
C
Institute of Physiological Chemistry, Ruhy-University Bochum, FRG.
Schoepper
B
B
Wegner
A
A
D051339:Actin Depolymerizing Factors; D000199:Actins / Q000032:analysis*; D000818:Animals; D001665:Binding Sites / Q000187:drug effects; D051345:Destrin; D008840:Microfilament Proteins / Q000037:antagonists & inhibitors; D009210:Myofibrils / Q000032:analysis*; D011108:Polymers / Q000032:analysis; D011817:Rabbits; D012518:Sarcomeres / Q000032:analysis*; D014335:Tropomyosin / Q000494:pharmacology*; D014336:Troponin / Q000494:pharmacology*
D051339:Actin Depolymerizing Factors; D000199:Actins; D051345:Destrin; D008840:Microfilament Proteins; D011108:Polymers; D014335:Tropomyosin; D014336:Troponin